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Literature summary for 3.6.5.4 extracted from
- Domain organization in the 54-kDa subunit of the chloroplast signal recognition particle (2016), Biophys. J., 111, 1151-1162 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of C-terminally His6-tagged wild-type and mutant mature cpSRP54 (residues 76-564) in Escherichia coli strain BL21 Star | Arabidopsis thaliana |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S54C/K407C | site-directed mutagenesis, mutations S54C in the N-domain and K407C in the M-domain of cpSRP54r resulting in mutant cpSRP54S54C/K407C | Arabidopsis thaliana |
| V339N/L370N | site-directed mutagenesis, mutant cpSRP54V339N/L370N of the mature enyme | Arabidopsis thaliana |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| chloroplast | the chloroplast signal recognition particle (cpSRP) is a heterodimer composed of an evolutionarily conserved 54-kDa GTPase (cpSRP54) and a unique 43-kDa subunit (cpSRP43) responsible for delivering light harvesting chlorophyll binding protein to the thylakoid membrane | Arabidopsis thaliana | 9507 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Arabidopsis thaliana |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + H2O | Arabidopsis thaliana | - |
GDP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | P37107 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant C-terminally His6-tagged wild-type and mutant mature cpSRP54 (residues 76-564) from Escherichia coli strain BL21 Star | Arabidopsis thaliana |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Arabidopsis thaliana | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + H2O | - |
Arabidopsis thaliana | GDP + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 22400-25600, recombinant M-domain of subunit SRP54, SDS-PAGE and SAXS | Arabidopsis thaliana |
| heterodimer | the chloroplast signal recognition particle (cpSRP) is a heterodimer composed of an evolutionarily conserved 54-kDa GTPase (cpSRP54) and a unique 43-kDa subunit (cpSRP43) responsible for delivering light harvesting chlorophyll binding protein to the thylakoid membrane. Determination of in silico three-dimensional model of the structure of cpSRP54 by homology modeling using cytosolic homologues. Single-molecule Foerster resonance energy transfer experiments reveals the presence of at least two distinct conformations. Small angle X-ray scattering shows that the linking region among the GTPase (G-domain) and methionine-rich (M-domain) domains, an M-domain loop, and the cpSRP43 binding C-terminal extension of cpSRP54 are predominantly disordered. The linker and loop segments are observed to play an important role in organizing the domain arrangement of cpSRP54. Domain structure, overview. The orientation of the M-domain varies in different SRP54s and bacterial homologues Ffhs, structure comparisons of wild-type and mutants and enzyme from other species, detailed overview. Subunit cpSRP54 exists in at least two different conformations | Arabidopsis thaliana |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 54-kDa GTPase | - |
Arabidopsis thaliana |
| chloroplast signal recognition particle | - |
Arabidopsis thaliana |
| cpSRP | - |
Arabidopsis thaliana |
| cpSRP54 | - |
Arabidopsis thaliana |
| signal recognition particle 54 kDa protein | - |
Arabidopsis thaliana |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | deletion of the finger loop abolishes loading of the cpSRP cargo, light-harvesting chlorophyll binding protein | Arabidopsis thaliana |
| additional information | the chloroplast signal recognition particle (cpSRP) is a heterodimer composed of an evolutionarily conserved 54-kDa GTPase (cpSRP54) and a unique 43-kDa subunit (cpSRP43) responsible for delivering light harvesting chlorophyll binding protein to the thylakoid membrane. Determination of in silico three-dimensional model of the structure of cpSRP54 by homology modeling using cytosolic homologues, overview. Single-molecule Foerster resonance energy transfer experiments reveals the presence of at least two distinct conformations. Small angle X-ray scattering shows that the linking region among the GTPase (G-domain) and methionine-rich (M-domain) domains, an M-domain loop, and the cpSRP43 binding C-terminal extension of cpSRP54 are predominantly disordered. The linker and loop segments are observed to play an important role in organizing the domain arrangement of cpSRP54 | Arabidopsis thaliana |
| physiological function | important structural dynamics relevant to cpSRP54's role in the post- and co-translational signaling processes | Arabidopsis thaliana |
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